کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5504746 | 1400253 | 2017 | 24 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
S-nitrosylation of the IGF-1 receptor disrupts the cell proliferative action of IGF-1
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کلمات کلیدی
S-nitroso-cysteineIGF-1RSDSMMTSS-nitrosylationSNOCERKPI3KPAGEIRSIGF-13-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide - 3- (4،5-dimethylthiazol-2-yl) -2،5-difenyltetrazolium bromideMAPK - MAPKMTT - MTTpolyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدinsulin receptor substrate - انسولین بستر گیرندهinsulin-like growth factor-1 - انسولین مانند عامل رشد 1sodium dodecyl sulfate - سدیم دودسیل سولفاتInsulin-like growth factor - فاکتور رشد مانند انسولینphosphoinositide 3-kinase - فسفینوزیتید 3-کینازNitric oxide - نیتریک اکسیدSignal transduction - هدایت سیگنالmitogen-activated protein kinase - پروتئین کیناز فعال با mitogenExtracellular signal-regulated protein kinase - پروتئین کیناز کنترل شده سیگنال غیر سلولیInsulin-like growth factor-1 receptor - گیرنده فاکتور 1 رشد انسولین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The insulin-like growth factor 1 receptor (IGF-1R) is a disulfide-linked heterotetramer containing two α-subunits and two β-subunits. Earlier studies demonstrate that nitric oxide (NO) can adversely affect IGF-1 action in the central nervous system. It is known that NO can induce S-nitrosylation of the cysteine residues in proteins, thereby partly contributing to the regulation of protein function. In the present study, we sought to determine whether S-nitrosylation of the cysteine residues in IGF-1R is an important post-translational modification that regulates its response to IGF-1. Using cultured SH-SY5Y human neuroblastoma cells as an in vitro model, we found that treatment of cells with S-nitroso-cysteine (SNOC), a NO donor that can nitrosylate the cysteine residues in proteins, induces S-nitrosylation of the β subunit of IGF-1R but not its α-subunit. IGF-1Rβ S-nitrosylation by SNOC is coupled with increased dissociation of the IGF-1R protein complex. In addition, disruption of the IGF-1R function resulting from S-nitrosylation of the IGF-1Rβ subunit is associated with disruption of the phosphoinositide 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) signaling pathways. Further, we observed that SNOC-induced IGF-1Rβ S-nitrosylation results in a dose-dependent inhibition of cell proliferation and survival. Together, these results suggest that elevated nitrosative stress may result in dysfunction of cellular IGF-1R signaling through S-nitrosylation of the cysteine residues in the IGF-1Rβ subunit, thereby disrupting the downstream PI3K and MAPK signaling functions and ultimately resulting in inhibition of cell proliferation and survival.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 491, Issue 4, 30 September 2017, Pages 870-875
Journal: Biochemical and Biophysical Research Communications - Volume 491, Issue 4, 30 September 2017, Pages 870-875
نویسندگان
Kazushi Okada, Bao-Ting Zhu,